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Database: UniProt
Entry: A0A0K2H1Y7_9CORY
LinkDB: A0A0K2H1Y7_9CORY
Original site: A0A0K2H1Y7_9CORY 
ID   A0A0K2H1Y7_9CORY        Unreviewed;       210 AA.
AC   A0A0K2H1Y7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Carbonic anhydrase {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE            EC=4.2.1.1 {ECO:0000256|ARBA:ARBA00012925, ECO:0000256|RuleBase:RU003956};
DE   AltName: Full=Carbonate dehydratase {ECO:0000256|RuleBase:RU003956};
GN   ORFNames=CLAC_10695 {ECO:0000313|EMBL:ALA68060.1};
OS   Corynebacterium lactis RW2-5.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1408189 {ECO:0000313|EMBL:ALA68060.1, ECO:0000313|Proteomes:UP000058446};
RN   [1] {ECO:0000313|EMBL:ALA68060.1, ECO:0000313|Proteomes:UP000058446}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RW2-5 {ECO:0000313|EMBL:ALA68060.1,
RC   ECO:0000313|Proteomes:UP000058446};
RA   Ruckert C., Albersmeier A., Lipski A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium lactis DSM 45799(T), isolated
RT   from raw cow milk.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide to form
CC       bicarbonate. {ECO:0000256|ARBA:ARBA00024993}.
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC       {ECO:0000256|RuleBase:RU003956}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000943,
CC         ECO:0000256|RuleBase:RU003956};
CC   -!- SIMILARITY: Belongs to the beta-class carbonic anhydrase family.
CC       {ECO:0000256|ARBA:ARBA00006217, ECO:0000256|RuleBase:RU003956}.
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DR   EMBL; CP006841; ALA68060.1; -; Genomic_DNA.
DR   RefSeq; WP_053412868.1; NZ_CP006841.1.
DR   AlphaFoldDB; A0A0K2H1Y7; -.
DR   STRING; 1408189.CLAC_10695; -.
DR   KEGG; clw:CLAC_10695; -.
DR   PATRIC; fig|1408189.4.peg.2152; -.
DR   OrthoDB; 9797527at2; -.
DR   Proteomes; UP000058446; Chromosome.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR   CDD; cd03378; beta_CA_cladeC; 1.
DR   Gene3D; 3.40.1050.10; Carbonic anhydrase; 1.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR015892; Carbonic_anhydrase_CS.
DR   InterPro; IPR036874; Carbonic_anhydrase_sf.
DR   PANTHER; PTHR11002; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR11002:SF13; CARBONIC ANHYDRASE 2; 1.
DR   Pfam; PF00484; Pro_CA; 1.
DR   SMART; SM00947; Pro_CA; 1.
DR   SUPFAM; SSF53056; beta-carbonic anhydrase, cab; 1.
DR   PROSITE; PS00705; PROK_CO2_ANHYDRASE_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003956};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003956}.
SQ   SEQUENCE   210 AA;  22695 MW;  4B30DA7A5E7CF724 CRC64;
     MSNSEWTPES VWQSIIRGNR RFVEGKSAHP RQNEGRRQEL THGQKPKAVV LACSDSRVPV
     EIIFDQGLGD IFVIRTAGEI TDLSVLASLE FAVDGLGVKL VVVLGHESCG AVAAAKSALD
     GGDLPGGFQR VLIEKVTPSL LAARKDGQHT TDEFERRHVQ EIVNHIVDRS PEISSRLDAG
     EVGVVGLRYR LSDGLAETVV TQGVSENPLP
//
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